reviewFrontiers in Molecular BiosciencesMar 12, 2019GOLD OA

Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1

Imperial College London

PubMed
Indexed incrossrefdoajpubmed

Abstract

The endoplasmic reticulum (ER) is an important site for protein folding and maturation in eukaryotes. The cellular requirement to synthesize proteins within the ER is matched by its folding capacity. However, the physiological demands or aberrations in folding may result in an imbalance which can lead to the accumulation of misfolded protein, also known as "ER stress." The unfolded protein response (UPR) is a cell-signaling system that readjusts ER folding capacity to restore protein homeostasis. The key UPR signal activator, IRE1, responds to stress by propagating the UPR signal from the ER to the cytosol. Here, we discuss the structural and molecular basis of IRE1 stress signaling, with particular focus on…

Citation impact

522
total citations
FWCI
29.56
Percentile
100%
References
90
Citations per year

Authors

5

Topics & keywords

Keywords
  • Unfolded protein response
  • Activator (genetics)
  • Mechanism (biology)
  • Signal transduction
  • Cell biology
  • Fight-or-flight response
  • Chemistry
  • Protein folding
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